Literature DB >> 16446278

Discovering motif pairs at interaction sites from protein sequences on a proteome-wide scale.

Haiquan Li1, Jinyan Li, Limsoon Wong.   

Abstract

MOTIVATION: Protein-protein interaction, mediated by protein interaction sites, is intrinsic to many functional processes in the cell. In this paper, we propose a novel method to discover patterns in protein interaction sites. We observed from protein interaction networks that there exist a kind of significant substructures called interacting protein group pairs, which exhibit an all-versus-all interaction between the two protein-sets in such a pair. The full-interaction between the pair indicates a common interaction mechanism shared by the proteins in the pair, which can be referred as an interaction type. Motif pairs at the interaction sites of the protein group pairs can be used to represent such interaction type, with each motif derived from the sequences of a protein group by standard motif discovery algorithms. The systematic discovery of all pairs of interacting protein groups from large protein interaction networks is a computationally challenging problem. By a careful and sophisticated problem transformation, the problem is solved using efficient algorithms for mining frequent patterns, a problem extensively studied in data mining.
RESULTS: We found 5349 pairs of interacting protein groups from a yeast interaction dataset. The expected value of sequence identity within the groups is only 7.48%, indicating non-homology within these protein groups. We derived 5343 motif pairs from these group pairs, represented in the form of blocks. Comparing our motifs with domains in the BLOCKS and PRINTS databases, we found that our blocks could be mapped to an average of 3.08 correlated blocks in these two databases. The mapped blocks occur 4221 out of total 6794 domains (protein groups) in these two databases. Comparing our motif pairs with iPfam consisting of 3045 interacting domain pairs derived from PDB, we found 47 matches occurring in 105 distinct PDB complexes. Comparing with another putative domain interaction database InterDom, we found 203 matches. AVAILABILITY: http://research.i2r.a-star.edu.sg/BindingMotifPairs/resources. SUPPLEMENTARY INFORMATION: http://research.i2r.a-star.edu.sg/BindingMotifPairs and Bioinformatics online.

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Year:  2006        PMID: 16446278     DOI: 10.1093/bioinformatics/btl020

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


  12 in total

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6.  Generative probabilistic models for protein-protein interaction networks--the biclique perspective.

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7.  Computing the protein binding sites.

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Journal:  BMC Bioinformatics       Date:  2012-06-25       Impact factor: 3.169

8.  'Double water exclusion': a hypothesis refining the O-ring theory for the hot spots at protein interfaces.

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Journal:  Bioinformatics       Date:  2009-01-29       Impact factor: 6.937

9.  Critical assessment of sequence-based protein-protein interaction prediction methods that do not require homologous protein sequences.

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Journal:  BMC Bioinformatics       Date:  2009-12-14       Impact factor: 3.169

10.  Triangle network motifs predict complexes by complementing high-error interactomes with structural information.

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Journal:  BMC Bioinformatics       Date:  2009-06-27       Impact factor: 3.169

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